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Simple parameterization of non‐proteinogenic amino acids for QSAR of antibacterial peptides
Author(s) -
Lejon Tore,
Svendsen John S.,
Haug Bengt E.
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.403
Subject(s) - amino acid , chemistry , escherichia coli , quantitative structure–activity relationship , aromatic amino acids , phenylalanine , antibacterial activity , biochemistry , staphylococcus aureus , peptide , combinatorial chemistry , stereochemistry , bacteria , biology , genetics , gene
Abstract The antibacterial activity of bovine lactoferricin‐(17–31)‐pentadecapeptide against Escherichia coli and Staphylococcus aureus is sensitive to substitution of the Trp residues, and synthetic peptides with phenylalanine and any of eight non‐proteinogenic aromatic amino acids greatly affected antibiotic activity. Using simple size‐related descriptors for the new amino acids it is possible to develop quantitative structure–activity relationships (QSARs) that can be used as tools in the search for more active peptides. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.